Matching Observed Alpha Helix Lengths to Predicted Secondary Structure

Published

November 1, 2009

Author(s)

Brian D. Cloteaux, Nadezhda Serova

Abstract

Because of the complexity in determining the 3D structure of a protein, the use of partial information determined from experimental techniques can greatly reduce the overall computational expense. We investigate the problem of matching experimentally observed lengths of helices to the predicted secondary structure of a protein. We give a simple and fast algorithm for producing a library of possible solutions. Then we test our algorithm by performing a series of computational experiments of predicting the alpha helix placement of proteins with an already known order. These tests seem to demonstrate that our method, if given a good prediction of the protein s secondary structure, can generate high quality lists of potential placements of the helix length onto the protein sequences.

Proceedings Title

Computational Structural Bioinformatics Workshop

Conference Dates

November 1-4, 2009

Conference Location

Washington, DC

Pub Type

Conferences

Download Paper

Local Download

Keywords

protein structure, randomized algorithm

Citation

Cloteaux, B. and Serova, N. (2009), Matching Observed Alpha Helix Lengths to Predicted Secondary Structure, Computational Structural Bioinformatics Workshop, Washington, DC, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=903670 (Accessed October 3, 2024)